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The oligomeric conformation of peroxiredoxins links redox state to function
Author(s) -
Barranco-Medina Sergio,
Lázaro Juan-José,
Dietz Karl-Josef
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.05.029
Subject(s) - redox , chaperone (clinical) , activator (genetics) , context (archaeology) , biophysics , chemistry , peroxidase , microbiology and biotechnology , function (biology) , biochemistry , enzyme , biology , receptor , medicine , paleontology , organic chemistry , pathology
Protein–protein associations, i.e. formation of permanent or transient protein complexes, are essential for protein functionality and regulation within the cellular context. Peroxiredoxins (Prx) undergo major redox‐dependent conformational changes and the dynamics are linked to functional switches. While a large number of investigations have addressed the principles and functions of Prx oligomerization, understanding of the diverse in vivo roles of this conserved redox‐dependent feature of Prx is slowly emerging. The review summarizes studies on Prx oligomerization, its tight connection to the redox state, and the knowledge and hypotheses on its physiological function in the cell as peroxidase, chaperone, binding partner, enzyme activator and/or redox sensor.